Modeling the active site chemistry of liver alcohol dehydrogenase: Mononuclear zinc methanol and N,N-Dimethylformamide complexes of a nitrogen/sulfurligand possessing an internal hydrogen bond donor
Lm. Berreau et al., Modeling the active site chemistry of liver alcohol dehydrogenase: Mononuclear zinc methanol and N,N-Dimethylformamide complexes of a nitrogen/sulfurligand possessing an internal hydrogen bond donor, INORG CHEM, 40(10), 2001, pp. 2212
Using a novel nitrogen/sulfur ligand possessing a single internal hydrogen
bond donor (bmapa, N,N-bis-(2-methylthio)ethyl-N-(6-amino-2-pyridylmethyl)-
amine), mononuclear zinc complexes possessing a single zinc-bound methanol
([(bmapa)Zn(MeOH)]-(ClO4)(2) . MeOH, 1 . MeOH) or N,N-dimethylformamide ([
(bmapa)Zn(DMF)](ClO4)(2), 2) molecule have been synthesized and structurall
y characterized. These complexes are structurally relevant to substrate- an
d inhibitor-bound forms of liver alcohol dehydrogenase (LADH) and exhibit h
ydrogen-bonding interactions akin to those found in the active site of LADH
.